Template-Type: ReDIF-Article 1.0
Author-Name: Naseem Ahmed
Author-Workplace-Name: Department of Chemistry, Govt. Degree College, Thannamandi 185212, J&K, India
Title: Biomolecular Interactions of Aromatic Amino Acids in Phosphate Buffer-Urea Systems: A Viscometric Analysis of DL-Phenylalanine, L-Tryptophan, and L-Tyrosine at Physiological Temperatures
Abstract: The relative and specific viscosities of three aromatic amino acids—DL-phenylalanine, L-tryptophan, and L-tyrosine—were measured in phosphate buffer solutions (pH 6, 7, and 8) containing 0.1 M aqueous urea at temperatures ranging from 303.15 to 328.15 K. The concentration of amino acids varied from 0.01 to 0.09 mol/kg. Absolute viscosities (η), solvent flow times (t₀), and Jones-Dole B-coefficients were determined to elucidate solute-solvent interactions. The results show that viscosity increases with amino acid concentration and decreases with temperature. L-tryptophan exhibits the highest viscosity values among the three amino acids studied, followed by L-tyrosine and DL-phenylalanine. The pH of the buffer solution significantly affects the viscometric behavior, with pH 8 generally showing higher viscosity values compared to pH 6 and 7. Temperature-dependent activation energies were calculated using Arrhenius analysis, revealing distinct energetic barriers for viscous flow in different amino acid systems. These findings provide valuable insights into biomolecular interactions, protein folding mechanisms, and the solution behavior of aromatic amino acids in biological buffer systems.
Keywords: viscometry, aromatic amino acids, phosphate buffer, Jones-Dole equation, protein stability
Journal: Inventum Biologicum: An International Journal of Biological Research
Pages: 35-41
Volume: 6
Issue: 1
Year: 2026
File-URL: https://journals.worldbiologica.com/ib/article/view/203
File-Format: text/html
File-URL: https://journals.worldbiologica.com/ib/article/view/203/371
File-Format: Application/pdf
Handle: RePEc:adg:ibijbr:v:6:y:2026:i:1:p:35-41